Calcium binding to a disordered domain of a type III-secreted protein from a coral pathogen promotes secondary structure formation and catalytic activity

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dc.identifier.uri http://dx.doi.org/10.15488/5060
dc.identifier.uri https://www.repo.uni-hannover.de/handle/123456789/5104
dc.contributor.author Hoyer, Elisabeth
dc.contributor.author Knöppel, Julius
dc.contributor.author Liebmann, Martina
dc.contributor.author Steppert, Michael
dc.contributor.author Raiwa, Manuel
dc.contributor.author Herczynski, Olivia
dc.contributor.author Hanspach, Erik
dc.contributor.author Zehner, Susanne
dc.contributor.author Göttfert, Michael
dc.contributor.author Tsushima, Satoru
dc.contributor.author Fahmy, Karim
dc.contributor.author Oertel, Jana
dc.date.accessioned 2019-07-02T07:58:21Z
dc.date.available 2019-07-02T07:58:21Z
dc.date.issued 2019
dc.identifier.citation Hoyer, E.; Knöppel, J.; Liebmann, M.; Steppert, M.; Raiwa, M. et al.: Calcium binding to a disordered domain of a type III-secreted protein from a coral pathogen promotes secondary structure formation and catalytic activity. In: Scientific Reports 9 (2019), Nr. 1, 7115. DOI: https://doi.org/10.1038/s41598-019-42898-0
dc.description.abstract Strains of the Gram-negative bacterium Vibrio coralliilyticus cause the bleaching of corals due to decomposition of symbiotic microalgae. The V. coralliilyticus strain ATCC BAA-450 (Vc450) encodes a type III secretion system (T3SS). The gene cluster also encodes a protein (locus tag VIC_001052) with sequence homology to the T3SS-secreted nodulation proteins NopE1 and NopE2 of Bradyrhizobium japonicum (USDA110). VIC_001052 has been shown to undergo auto-cleavage in the presence of Ca 2+ similar to the NopE proteins. We have studied the hitherto unknown secondary structure, Ca 2+ -binding affinity and stoichiometry of the “metal ion-inducible autocleavage” (MIIA) domain of VIC_001052 which does not possess a classical Ca 2+ -binding motif. CD and fluorescence spectroscopy revealed that the MIIA domain is largely intrinsically disordered. Binding of Ca 2+ and other di- and trivalent cations induced secondary structure and hydrophobic packing after partial neutralization of the highly negatively charged MIIA domain. Mass spectrometry and isothermal titration calorimetry showed two Ca 2+ -binding sites which promote structure formation with a total binding enthalpy of −110 kJ mol −1 at a low micromolar K d . Putative binding motifs were identified by sequence similarity to EF-hand domains and their structure analyzed by molecular dynamics simulations. The stoichiometric Ca 2+ -dependent induction of structure correlated with catalytic activity and may provide a “host-sensing” mechanism that is shared among pathogens that use a T3SS for efficient secretion of disordered proteins. eng
dc.language.iso eng
dc.publisher London : Nature Publishing Group
dc.relation.ispartofseries Scientific Reports 9 (2019), Nr. 1
dc.rights CC BY 4.0 Unported
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject Calcium eng
dc.subject protein eng
dc.subject CA2+ eng
dc.subject stoichiometry eng
dc.subject.ddc 500 | Naturwissenschaften ger
dc.subject.ddc 600 | Technik ger
dc.title Calcium binding to a disordered domain of a type III-secreted protein from a coral pathogen promotes secondary structure formation and catalytic activity eng
dc.type article
dc.type Text
dc.relation.issn 2045-2322
dc.relation.doi https://doi.org/10.1038/s41598-019-42898-0
dc.bibliographicCitation.issue 1
dc.bibliographicCitation.volume 9
dc.bibliographicCitation.firstPage 7115
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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